1FWM
Crystal structure of the thymidylate synthase R166Q mutant
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0003723 | molecular_function | RNA binding |
A | 0004799 | molecular_function | thymidylate synthase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006231 | biological_process | dTMP biosynthetic process |
A | 0006235 | biological_process | dTTP biosynthetic process |
A | 0006417 | biological_process | regulation of translation |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0009165 | biological_process | nucleotide biosynthetic process |
A | 0009314 | biological_process | response to radiation |
A | 0016741 | molecular_function | transferase activity, transferring one-carbon groups |
A | 0032259 | biological_process | methylation |
A | 0042803 | molecular_function | protein homodimerization activity |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0003723 | molecular_function | RNA binding |
B | 0004799 | molecular_function | thymidylate synthase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006231 | biological_process | dTMP biosynthetic process |
B | 0006235 | biological_process | dTTP biosynthetic process |
B | 0006417 | biological_process | regulation of translation |
B | 0008168 | molecular_function | methyltransferase activity |
B | 0009165 | biological_process | nucleotide biosynthetic process |
B | 0009314 | biological_process | response to radiation |
B | 0016741 | molecular_function | transferase activity, transferring one-carbon groups |
B | 0032259 | biological_process | methylation |
B | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 265 |
Chain | Residue |
A | ARG21 |
A | SER167 |
A | CB3266 |
A | HOH641 |
B | ARG426 |
B | ARG427 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 565 |
Chain | Residue |
B | ARG321 |
B | SER467 |
B | CB3566 |
A | ARG126 |
A | ARG127 |
A | HOH616 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE CB3 A 266 |
Chain | Residue |
A | GLU58 |
A | ILE79 |
A | TRP80 |
A | TRP83 |
A | TYR94 |
A | LEU143 |
A | ALA144 |
A | CYS146 |
A | PHE176 |
A | ASN177 |
A | LYS259 |
A | VAL262 |
A | SO4265 |
A | HOH635 |
A | HOH639 |
A | HOH692 |
A | HOH732 |
site_id | AC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CB3 B 566 |
Chain | Residue |
A | SO4565 |
B | HIS351 |
B | ILE379 |
B | TRP380 |
B | TRP383 |
B | TYR394 |
B | LEU443 |
B | ALA444 |
B | CYS446 |
B | GLY473 |
B | PHE476 |
B | ASN477 |
B | HOH620 |
B | HOH640 |
B | HOH753 |
Functional Information from PROSITE/UniProt
site_id | PS00091 |
Number of Residues | 29 |
Details | THYMIDYLATE_SYNTHASE Thymidylate synthase active site. RriIvsaWNvgeldkma.....LaPCHaffQFyV |
Chain | Residue | Details |
A | ARG126-VAL154 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00008, ECO:0000269|PubMed:2223754, ECO:0000269|PubMed:8973201, ECO:0000269|PubMed:9416600 |
Chain | Residue | Details |
A | CYS146 | |
B | CYS446 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: in other chain => ECO:0000269|PubMed:2223754, ECO:0000269|PubMed:8973201, ECO:0007744|PDB:1KCE, ECO:0007744|PDB:2TSC |
Chain | Residue | Details |
A | ARG21 | |
A | GLN166 | |
A | ASN177 | |
A | HIS207 | |
B | ARG321 | |
B | GLN466 | |
B | ASN477 | |
B | HIS507 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000305|PubMed:8312270, ECO:0007744|PDB:1TYS |
Chain | Residue | Details |
A | HIS51 | |
A | ASP169 | |
A | ALA263 | |
B | HIS351 | |
B | ASP469 | |
B | ALA563 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:2223754, ECO:0000269|PubMed:8973201, ECO:0007744|PDB:1KCE, ECO:0007744|PDB:2TSC |
Chain | Residue | Details |
A | ARG126 | |
B | ARG426 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1b02 |
Chain | Residue | Details |
A | HIS207 | |
A | GLU58 | |
A | ASP169 | |
A | SER167 | |
A | CYS146 | |
A | ASP205 |
site_id | CSA2 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1b02 |
Chain | Residue | Details |
B | ASP469 | |
B | SER467 | |
B | HIS507 | |
B | ASP505 | |
B | GLU358 | |
B | CYS446 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b02 |
Chain | Residue | Details |
A | SER180 | |
A | ASN177 | |
A | CYS146 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b02 |
Chain | Residue | Details |
B | SER480 | |
B | CYS446 | |
B | ASN477 |